dc.contributor.author | Ogoyi, Dorington O. | |
dc.contributor.author | Osir, Ellie O. | |
dc.contributor.author | Olembo, Norah K. | |
dc.date.accessioned | 2013-06-26T06:00:56Z | |
dc.date.available | 2013-06-26T06:00:56Z | |
dc.date.issued | 1995-11 | |
dc.identifier.citation | Ogoyi, Dorington O, Olembo, Norah K. P Osir, Ellie O .Comparative Biochemistry and Physiology Part B :Biochemistry and Molecular Biology Volume 112, Issue 3, November 1995, Pages 441–449 | en |
dc.identifier.uri | http://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/40032 | |
dc.description.abstract | Lipophorin was isolated from the hemolymph by KBr density gradient ultracentrifugation. Apolipophorin-III (apoLp-III) was isolated from low-density lipophorin (LDLp). High-density lipophorin (HDLp) (Mr ∼-620,000) consisted of two apoproteins, apoLp-I (Mr ∼-224,000) and apoLp-II (Mr ∼-81,000). Isolated apoLp-III (Mr ∼-20,000) had two isoforms in non-denaturing gels. Injection of adipokinetic hormone-I resulted in the formation of LDLp in both locust phases. Lipid content of HDLp was estimated at 48.4% and 51.8% for solitary and gregarious locusts, respectively. In LDLp, lipids constituted 59.8% and 57.1% for gregarious and solitary locusts, respectively. The results suggest that the gregarious locusts were more efficient in the conversion of HDLp to LDLp. | en |
dc.language.iso | en | en |
dc.publisher | University of Nairobi | en |
dc.title | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology | en |
dc.type | Article | en |
local.publisher | Department of Biochemistry, University of Nairobi | en |